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Database: UniProt
Entry: A0A1Y1WWY3_9FUNG
LinkDB: A0A1Y1WWY3_9FUNG
Original site: A0A1Y1WWY3_9FUNG 
ID   A0A1Y1WWY3_9FUNG        Unreviewed;      1083 AA.
AC   A0A1Y1WWY3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Chitin-binding type-1 domain-containing protein {ECO:0000259|PROSITE:PS50941};
GN   ORFNames=BCR32DRAFT_283014 {ECO:0000313|EMBL:ORX77644.1};
OS   Anaeromyces robustus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Anaeromyces.
OX   NCBI_TaxID=1754192 {ECO:0000313|EMBL:ORX77644.1, ECO:0000313|Proteomes:UP000193944};
RN   [1] {ECO:0000313|EMBL:ORX77644.1, ECO:0000313|Proteomes:UP000193944}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4 {ECO:0000313|EMBL:ORX77644.1,
RC   ECO:0000313|Proteomes:UP000193944};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ORX77644.1, ECO:0000313|Proteomes:UP000193944}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4 {ECO:0000313|EMBL:ORX77644.1,
RC   ECO:0000313|Proteomes:UP000193944};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORX77644.1}.
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DR   EMBL; MCFG01000240; ORX77644.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1WWY3; -.
DR   STRING; 1754192.A0A1Y1WWY3; -.
DR   OrthoDB; 1340441at2759; -.
DR   Proteomes; UP000193944; Unassembled WGS sequence.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00035; ChtBD1; 2.
DR   CDD; cd00161; RICIN; 3.
DR   Gene3D; 2.80.10.50; -; 5.
DR   Gene3D; 3.30.60.10; Endochitinase-like; 4.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR036861; Endochitinase-like_sf.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR46471; CHITIN DEACETYLASE; 1.
DR   PANTHER; PTHR46471:SF2; CHITIN DEACETYLASE-RELATED; 1.
DR   Pfam; PF00187; Chitin_bind_1; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 3.
DR   SMART; SM00270; ChtBD1; 4.
DR   SMART; SM00458; RICIN; 5.
DR   SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 4.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 6.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR   PROSITE; PS50941; CHIT_BIND_I_2; 4.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 3.
PE   4: Predicted;
KW   Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW   ProRule:PRU00261};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00261}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193944};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1083
FT                   /note="Chitin-binding type-1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012395224"
FT   DOMAIN          300..342
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50941"
FT   DOMAIN          635..677
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50941"
FT   DOMAIN          1000..1039
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50941"
FT   DOMAIN          1040..1083
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50941"
FT   REGION          695..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        310..322
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        315..329
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        645..657
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        650..664
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        1009..1021
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        1014..1028
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        1054..1068
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   1083 AA;  122038 MW;  00DB1BFC99D1EFCB CRC64;
     MKNHFLFFTI STFFNYLFDS ANASSNVPRY VYNPYTKKCL MAPSGSNKKV LVQDCENNSK
     FRWLVTTDSE DFFRSEFSNS NCLNLIDIDN GLLEVSKCEE NNLMLFSNDG FIYSSSSTDE
     YCMGVGDGEP ENENTVFFKE CEMIDDQQWE LWGKNPIDIV NAKTQKVWIY NEILDKCLYS
     GTTINSKPII ADCDDTNRAK WEVSISGDSF FRSLNKRMCL TVNNINTGAI VMGNCNGNSV
     ITDINSTYNK ESIMSSQSNE MCLGLMESNN PNETRLSLIK CDASKNDQHW KIYTNNPNDF
     AKCGPIKGQC PSGQCCNKNG ICGTTSDFCN EGCQQKYGKC NVKTTTTTTT TTTTTTRTVL
     PTDDSEQDLT PKWIYNEYTD KCLYAQLTTN KKPMLKSCQD SIRFQWLTTP YPKGRFISKA
     NESRCLRITD PESGELKVGT CKDDDIFEIT YDGVIYSSSI SDEFCMSVSE EDDTAYFKEC
     DMIEGQIWTL WDRNPYEIVK AETHEVWIYN KKLDKCLYSG TYFNDKPTIG DCNDNNRNKW
     IVPVSGDGFY KSLSKKYCLN VNNINSGSIV MGTCDNNAII SDITFSYNKE SITSPLDESK
     CLGFDSSNNS KLRLNKCNKN NDDQHWEIRT TNPSIIKCGA GIGNCPSGQC CSKDGICGTS
     NDFCGSGCQS KFGKCNITTT TTTRTTTTRT TTTTTTTTTT TTTTTTTTTT TTTTTTTTMK
     GAPTVNPNAT PKWIYNPSAK ICLWALSAID KKPRIWECGE DEDFKWYLSP YPKGYIYSAY
     YEGRCFTLMD PVNGKIKVSD CTKASSYEFN YSEGLLYLDN DYSKCMGIGD GDPTNDNGAY
     LRPCKKDADQ KWEIWDRNPS SVINADYQTV WIYNKYLNKC LLSGSKKTYR PIIGDCSNNN
     RSKWLIPVSG DGFIKSLYMP DTCINLSNAQ RGTLIMKDCN NEAVFLDINK NNERIISPIN
     NKCIGYYEND NTKLNLNTCD SNKEDQYWMI SKSNPYTHNN VRCSSNKFCP ENQCCSEDGY
     CGISNKHCGM GCQNGKCTLR CGSNFANQSC NQNCCSYYNW CGTSDDYCKI SSRCQPAYGR
     CIN
//
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